The dissociation constants of lanthanide-ATP complexes will be determined by the kinetic method of competition with Mg. Isotope effects with 15N-DPN will be looked for with dehydrogenases other than liver dehydrogenase to see if the mechanism involving bending of the nicotinamide-ribose bond is a general one. Primary and secondary deuterium, and primary 18O isotope effects will be measured with enolase by equilibrium perturbation to determine the chemical mechanism. Isotope effects will be measured with aconitase using methyl aconitate and methylisocitrate as substrates. The pH profiles for phosphorylation of pyruvate, glycolate and fluoride will be measured to determine the nature of any acid-base catalysts involved in the reaction. The chemistry of aldehyde-induced ATPase reactions will be studied to determine if the aldehydes are phosphorylated, or induce a metaphosphate cleavage of ATP.